P69786 · PTGCB_ECOLI

Function

function

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:10562420, PubMed:3129430).
Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc (PubMed:18319344).
In the presence of glucose in the medium, the dephosphorylated form of PtsG can interact with Mlc, leading to sequestration of Mlc in the inner membrane and inhibition of its repressor activity (PubMed:11032803, PubMed:11157755, PubMed:12529317, PubMed:18319344).
(Microbial infection) Probably transports the toxic C-terminal region of CdiA from E.coli strains NC101 and 3006 across the inner membrane to the cytoplasm, where CdiA degrades specific tRNAs. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins (PubMed:26305955).
Probably also serves as the inner membrane receptor for CdiA-STECO31 from E.coli strain STEC_O31 (Probable)

Catalytic activity

Activity regulation

Transporter activity may be inhibited by SgrT.

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site421Phosphocysteine intermediate; for EIIB activity

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentplasma membrane
Cellular Componenttransmembrane transporter complex
Molecular Functionglucose transmembrane transporter activity
Molecular Functionkinase activity
Molecular Functionprotein-N(PI)-phosphohistidine-sugar phosphotransferase activity
Molecular Functionprotein-phosphocysteine-glucose phosphotransferase system transporter activity
Biological Processglucose import across plasma membrane
Biological Processglucose transmembrane transport
Biological Processphosphoenolpyruvate-dependent sugar phosphotransferase system
Biological Processregulation of DNA-templated transcription

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    PTS system glucose-specific EIICB component
  • Alternative names
    • EIICB-Glc
      (EII-Glc
      )

Including 2 domains:

  • Recommended name
    Glucose permease IIC component
  • Alternative names
    • PTS system glucose-specific EIIC component
  • Recommended name
    Glucose-specific phosphotransferase enzyme IIB component
  • EC number
  • Alternative names
    • PTS system glucose-specific EIIB component

Gene names

    • Name
      ptsG
    • Synonyms
      glcA, umg
    • Ordered locus names
      b1101, JW1087

Organism names

  • Taxonomic identifier
  • Strains
    • K12
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P69786
  • Secondary accessions
    • P05053

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-14Cytoplasmic
Transmembrane15-35Helical
Topological domain36-50Periplasmic
Transmembrane51-71Helical
Topological domain72-79Cytoplasmic
Transmembrane80-100Helical
Topological domain101-111Periplasmic
Transmembrane112-132Helical
Topological domain133-151Cytoplasmic
Transmembrane152-172Helical
Topological domain173-190Periplasmic
Transmembrane191-211Helical
Topological domain212-249Cytoplasmic
Transmembrane250-270Helical
Topological domain271-279Periplasmic
Transmembrane280-300Helical
Topological domain301-309Cytoplasmic
Transmembrane310-330Helical
Topological domain331-355Periplasmic
Transmembrane356-376Helical
Topological domain377-477Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

Disruption confers resistance to cellular contact-dependent growth inhibition (CDI) CdiA of E.coli strains NC101 and 3006, but not to several other tested CdiA toxins (PubMed:26305955).
Disruption confers resistance to cellular contact-dependent growth inhibition (CDI) CdiA-STECO31 of E.coli strain STEC_O31 (PubMed:28351921).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis204Destabilizes the protein structure; when associated with S-326.
Mutagenesis326Destabilizes the protein structure; when associated with S-204.
Mutagenesis419Still allows binding to Mlc.
Mutagenesis421Still allows binding to Mlc. Derepression of Mlc targets becomes constitutive, i.e. independent of PTS phosphorylation.
Mutagenesis421Unable to be phosphorylated and to catalyze the phosphoryl exchange between glucose and glucose 6-phosphate at equilibrium. Remains susceptible to CdiA toxin from E.coli strain 3006. Still allows binding to Mlc. Derepression of Mlc targets becomes constitutive, i.e. independent of PTS phosphorylation.
Mutagenesis422Still allows binding to Mlc.
Mutagenesis423Decreases Mlc binding.
Mutagenesis424Cannot bind Mlc. Destroys the ability of Cys-421 to be phosphorylated in vitro.
Mutagenesis424Cannot bind Mlc. Cys-421 can be phosphorylated in vitro.
Mutagenesis426Still allows binding to Mlc. Cys-421 is weakly phosphorylated in vitro.
Mutagenesis449Interaction with Mlc is hardly detectable.
Mutagenesis451The complex with Mlc shows much weaker association than the wild-type.
Mutagenesis456Decreases Mlc binding. Interaction with Mlc is hardly detectable.
Mutagenesis458Still allows binding to Mlc.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001865281-477PTS system glucose-specific EIICB component
Modified residue421Phosphocysteine

Keywords

Proteomic databases

PTM databases

Expression

Induction

Induced by glucose (PubMed:9781886).
Expression is positively regulated by the cAMP-CRP complex and negatively regulated by the Mlc transcriptional repressor (PubMed:9781886).
Mlc and CRP-cAMP bind independently to the ptsG promoter region, and the action of Mlc is dominant over the cAMP-CRP action (PubMed:9781886).
The ptsG transcript is degraded under conditions of glucose-phosphate stress (due to intracellular accumulation of glucose-6-phosphate caused by disruption of glycolytic flux), or in the presence of (toxic) non-metabolizable glucose phosphate analogs due to hybridization with the small RNA sgrS (originally known as ryaA). This hybridization is sufficient to repress mRNA translation. The hybrid is subsequently degraded by RNase E. This reduces the quantity of transporter and relieves glucose phosphate stress (PubMed:15522088, PubMed:16549791).

Interaction

Subunit

Homodimer (Probable) (PubMed:10562420, PubMed:12716891, PubMed:18319344).
The dephosphorylated form interacts with the Mlc transcriptional repressor (PubMed:11032803, PubMed:11157755, PubMed:12529317, PubMed:18319344).
Mlc and the EIIB domain form a complex with the 1:1 stoichiometry (PubMed:18319344).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P69786mlc P504563EBI-903497, EBI-1116104
View interactors in UniProtKB
View CPX-2242 in Complex Portal

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-388PTS EIIC type-1
Domain399-477PTS EIIB type-1

Domain

The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Initial studies suggest that binding to Mlc requires the EIIB domain and the EIIC-B junction region, or that the soluble EIIB domain is sufficient (PubMed:11032803, PubMed:11157755).
A more recent study shows that the soluble EIIB domain is sufficient to interact with Mlc but only when EIIB is attached to the membrane by a protein anchor (PubMed:12529317).

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    477
  • Mass (Da)
    50,677
  • Last updated
    1987-08-13 v1
  • Checksum
    D97A80FD64B74F73
MFKNAFANLQKVGKSLMLPVSVLPIAGILLGVGSANFSWLPAVVSHVMAEAGGSVFANMPLIFAIGVALGFTNNDGVSALAAVVAYGIMVKTMAVVAPLVLHLPAEEIASKHLADTGVLGGIISGAIAAYMFNRFYRIKLPEYLGFFAGKRFVPIISGLAAIFTGVVLSFIWPPIGSAIQTFSQWAAYQNPVVAFGIYGFIERCLVPFGLHHIWNVPFQMQIGEYTNAAGQVFHGDIPRYMAGDPTAGKLSGGFLFKMYGLPAAAIAIWHSAKPENRAKVGGIMISAALTSFLTGITEPIEFSFMFVAPILYIIHAILAGLAFPICILLGMRDGTSFSHGLIDFIVLSGNSSKLWLFPIVGIGYAIVYYTIFRVLIKALDLKTPGREDATEDAKATGTSEMAPALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGVQAIFGTKSDNLKTEMDEYIRNH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J02618
EMBL· GenBank· DDBJ
AAA24437.1
EMBL· GenBank· DDBJ
Genomic DNA
U00096
EMBL· GenBank· DDBJ
AAC74185.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA35908.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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